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- W4377140347 abstract "Amyloid formation is a hallmark of various neurodegenerative disorders. In this contribution, energy landscapes are explored for various hexapeptides that are known to form amyloids. Heat capacity (C V ) analysis at low temperature for these hexapeptides reveals that the low energy structures contributing to the first heat capacity feature above a threshold temperature exhibit a variety of backbone conformations for amyloid forming monomers. The corresponding control sequences do not exhibit such structural polymorphism, as diagnosed via end-to-end distance and a dihedral angle defined for the monomer. A similar heat capacity analysis for dimer conformations obtained using basin-hopping global optimisation, shows clear features in end-to-end distance versus dihedral correlation plots, where amyloid-forming sequences exhibit a preference for larger end-to-end distances and larger positive dihedrals. These results hold for sequences taken from tau, amylin, insulin A chain, a de-novo designed peptide, and various control sequences. While there is a little overall correlation between the aggregation propensity and the temperature at which the low-temperature C V feature occurs, further analysis suggests that the amyloid forming sequences exhibit the key C V feature at a lower temperature compared to control sequences derived from the same protein." @default.
- W4377140347 created "2023-05-21" @default.
- W4377140347 creator A5014057135 @default.
- W4377140347 creator A5022301289 @default.
- W4377140347 date "2023-05-19" @default.
- W4377140347 modified "2023-09-30" @default.
- W4377140347 title "Energy landscapes and heat capacity signatures for monomers and dimers of amyloid forming hexapeptides" @default.
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- W4377140347 doi "https://doi.org/10.1101/2023.05.17.541223" @default.
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